当前位置: X-MOL 学术Annu. Rev. Biophys. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.
Annual Review of Biophysics ( IF 10.4 ) Pub Date : 2008-01-01 , DOI: 10.1146/annurev.biophys.37.032807.125842
Tom K Kerppola 1
Affiliation  

Protein interactions are a fundamental mechanism for the generation of biological regulatory specificity. The study of protein interactions in living cells is of particular significance because the interactions that occur in a particular cell depend on the full complement of proteins present in the cell and the external stimuli that influence the cell. Bimolecular fluorescence complementation (BiFC) analysis enables direct visualization of protein interactions in living cells. The BiFC assay is based on the association between two nonfluorescent fragments of a fluorescent protein when they are brought in proximity to each other by an interaction between proteins fused to the fragments. Numerous protein interactions have been visualized using the BiFC assay in many different cell types and organisms. The BiFC assay is technically straightforward and can be performed using standard molecular biology and cell culture reagents and a regular fluorescence microscope or flow cytometer.

中文翻译:

双分子荧光互补 (BiFC) 分析作为活细胞中蛋白质相互作用的探针。

蛋白质相互作用是产生生物调节特异性的基本机制。活细胞中蛋白质相互作用的研究具有特别重要的意义,因为在特定细胞中发生的相互作用取决于细胞中存在的蛋白质的完整补体以及影响细胞的外部刺激。双分子荧光互补 (BiFC) 分析能够直接可视化活细胞中的蛋白质相互作用。BiFC 测定基于荧光蛋白的两个非荧光片段之间的关联,当它们通过融合到片段的蛋白质之间的相互作用而彼此接近时。在许多不同的细胞类型和生物体中,使用附设分析法已经可视化了许多蛋白质相互作用。
更新日期:2019-11-01
down
wechat
bug